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. Author manuscript; available in PMC: 2015 Feb 1.
Published in final edited form as: Curr Opin Cell Biol. 2014 Jan 23;26:139–146. doi: 10.1016/j.ceb.2013.12.006

Table 1.

Protein Quality Control Compartments in Eukaryotic Cells

PQC
compartment
Conditions of appearance Substrates Cellular
localization
Sorting factors/
associated proteins
Solubility Cytoskeleton
dependency
References
Q-body mild-severe heat stress; no proteasome inhibition soluble, misfolded proteins cortical ER Hsp42, Hsp104, Hsp70, Hsp90, Hsp110, Ydj1/Hlj1 soluble no [10]
JUNQ severe heat stress; proteasome inhibition soluble, ubiquitylated, misfolded proteins juxtanuclear, perinuclear ER Sis1, Btn2, Hsp70 proteasome soluble yes, actin [1415,21]
IPOD normal growth conditions; no proteasome inhibition amyloid proteins perivacuolar Hsp42, Btn2 (not for prions) insoluble debated, actin [1415,21]
Aggresome proteasome inhibition ubiquitylated, misfolded proteins MTOC/SPB Hsc70, Hsp40; HDAC6, parkin, ataxin-3, ubiquilin-1 Insoluble (& soluble?) yes, microtubule [19]
ALIS wide range of stress conditions ubiquitylated, misfolded proteins peripheral and juxtanuclear ubiquitin; Atg8 soluble yes, microtubule and actin [22]
ERAC/ERQC genetic mutations that induce misfolding misfolded membrane proteins/ERAD substrates ER Kar2p soluble no [30]